JP2019503341A - 植物細胞に生物学的に封入された、治療用タンパク質の、疾患の治療のための関心のある細胞型への標的化された送達 - Google Patents
植物細胞に生物学的に封入された、治療用タンパク質の、疾患の治療のための関心のある細胞型への標的化された送達 Download PDFInfo
- Publication number
- JP2019503341A JP2019503341A JP2018525435A JP2018525435A JP2019503341A JP 2019503341 A JP2019503341 A JP 2019503341A JP 2018525435 A JP2018525435 A JP 2018525435A JP 2018525435 A JP2018525435 A JP 2018525435A JP 2019503341 A JP2019503341 A JP 2019503341A
- Authority
- JP
- Japan
- Prior art keywords
- gfp
- cells
- protein
- cell
- peptide
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 137
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 119
- 230000001225 therapeutic effect Effects 0.000 title claims abstract description 47
- 238000012384 transportation and delivery Methods 0.000 title claims description 57
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 title claims description 15
- 238000011282 treatment Methods 0.000 title claims description 12
- 201000010099 disease Diseases 0.000 title claims description 11
- 108020001507 fusion proteins Proteins 0.000 claims abstract description 74
- 102000037865 fusion proteins Human genes 0.000 claims abstract description 74
- 238000000034 method Methods 0.000 claims abstract description 36
- 210000004027 cell Anatomy 0.000 claims description 183
- 241000196324 Embryophyta Species 0.000 claims description 99
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 57
- 230000004927 fusion Effects 0.000 claims description 50
- 230000014509 gene expression Effects 0.000 claims description 33
- 150000007523 nucleic acids Chemical class 0.000 claims description 32
- 210000004443 dendritic cell Anatomy 0.000 claims description 31
- 210000001519 tissue Anatomy 0.000 claims description 28
- 102000039446 nucleic acids Human genes 0.000 claims description 27
- 108020004707 nucleic acids Proteins 0.000 claims description 27
- 210000002865 immune cell Anatomy 0.000 claims description 19
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 claims description 16
- 238000001727 in vivo Methods 0.000 claims description 10
- 108090001061 Insulin Proteins 0.000 claims description 9
- 102000004877 Insulin Human genes 0.000 claims description 8
- 229940125396 insulin Drugs 0.000 claims description 8
- 238000004519 manufacturing process Methods 0.000 claims description 8
- 102000004190 Enzymes Human genes 0.000 claims description 7
- 108090000790 Enzymes Proteins 0.000 claims description 7
- 210000002510 keratinocyte Anatomy 0.000 claims description 7
- 108700042778 Antimicrobial Peptides Proteins 0.000 claims description 6
- 102000044503 Antimicrobial Peptides Human genes 0.000 claims description 6
- 108091005804 Peptidases Proteins 0.000 claims description 6
- 229940088598 enzyme Drugs 0.000 claims description 6
- 210000002706 plastid Anatomy 0.000 claims description 6
- 102000014150 Interferons Human genes 0.000 claims description 5
- 108010050904 Interferons Proteins 0.000 claims description 5
- 240000008415 Lactuca sativa Species 0.000 claims description 5
- 235000003228 Lactuca sativa Nutrition 0.000 claims description 5
- 239000003114 blood coagulation factor Substances 0.000 claims description 5
- 239000000137 peptide hydrolase inhibitor Substances 0.000 claims description 5
- 240000007124 Brassica oleracea Species 0.000 claims description 4
- 235000003899 Brassica oleracea var acephala Nutrition 0.000 claims description 4
- 244000000626 Daucus carota Species 0.000 claims description 4
- 235000002767 Daucus carota Nutrition 0.000 claims description 4
- 108010051696 Growth Hormone Proteins 0.000 claims description 4
- 235000007688 Lycopersicon esculentum Nutrition 0.000 claims description 4
- 244000061176 Nicotiana tabacum Species 0.000 claims description 4
- 235000002637 Nicotiana tabacum Nutrition 0.000 claims description 4
- 240000003768 Solanum lycopersicum Species 0.000 claims description 4
- 208000007536 Thrombosis Diseases 0.000 claims description 4
- 230000007812 deficiency Effects 0.000 claims description 4
- 208000035475 disorder Diseases 0.000 claims description 4
- 230000023597 hemostasis Effects 0.000 claims description 4
- 229940079322 interferon Drugs 0.000 claims description 4
- 239000000843 powder Substances 0.000 claims description 4
- 210000001082 somatic cell Anatomy 0.000 claims description 4
- 102000013142 Amylases Human genes 0.000 claims description 3
- 108010065511 Amylases Proteins 0.000 claims description 3
- 102100026189 Beta-galactosidase Human genes 0.000 claims description 3
- 102000007350 Bone Morphogenetic Proteins Human genes 0.000 claims description 3
- 108010007726 Bone Morphogenetic Proteins Proteins 0.000 claims description 3
- 208000017701 Endocrine disease Diseases 0.000 claims description 3
- 102000003951 Erythropoietin Human genes 0.000 claims description 3
- 108090000394 Erythropoietin Proteins 0.000 claims description 3
- 102000012673 Follicle Stimulating Hormone Human genes 0.000 claims description 3
- 108010079345 Follicle Stimulating Hormone Proteins 0.000 claims description 3
- 108010017544 Glucosylceramidase Proteins 0.000 claims description 3
- 102000004547 Glucosylceramidase Human genes 0.000 claims description 3
- 102000004269 Granulocyte Colony-Stimulating Factor Human genes 0.000 claims description 3
- 108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 claims description 3
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 claims description 3
- 108010059881 Lactase Proteins 0.000 claims description 3
- 102000004882 Lipase Human genes 0.000 claims description 3
- 108090001060 Lipase Proteins 0.000 claims description 3
- 239000004367 Lipase Substances 0.000 claims description 3
- 102100024295 Maltase-glucoamylase Human genes 0.000 claims description 3
- 102000017975 Protein C Human genes 0.000 claims description 3
- 102000013275 Somatomedins Human genes 0.000 claims description 3
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 claims description 3
- 102000003978 Tissue Plasminogen Activator Human genes 0.000 claims description 3
- 108010028144 alpha-Glucosidases Proteins 0.000 claims description 3
- 235000019418 amylase Nutrition 0.000 claims description 3
- 239000004019 antithrombin Substances 0.000 claims description 3
- 108010005774 beta-Galactosidase Proteins 0.000 claims description 3
- 229940112869 bone morphogenetic protein Drugs 0.000 claims description 3
- 208000030172 endocrine system disease Diseases 0.000 claims description 3
- 229940105423 erythropoietin Drugs 0.000 claims description 3
- 229940028334 follicle stimulating hormone Drugs 0.000 claims description 3
- 229940116108 lactase Drugs 0.000 claims description 3
- 235000019421 lipase Nutrition 0.000 claims description 3
- 230000035515 penetration Effects 0.000 claims description 3
- 239000003910 polypeptide antibiotic agent Substances 0.000 claims description 3
- OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 claims description 3
- 235000019419 proteases Nutrition 0.000 claims description 3
- 229960000856 protein c Drugs 0.000 claims description 3
- 208000024891 symptom Diseases 0.000 claims description 3
- 229960000187 tissue plasminogen activator Drugs 0.000 claims description 3
- 235000011301 Brassica oleracea var capitata Nutrition 0.000 claims description 2
- 235000001169 Brassica oleracea var oleracea Nutrition 0.000 claims description 2
- 235000012905 Brassica oleracea var viridis Nutrition 0.000 claims description 2
- 102000004457 Granulocyte-Macrophage Colony-Stimulating Factor Human genes 0.000 claims description 2
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 claims description 2
- 101710111620 Protein C activator Proteins 0.000 claims description 2
- 244000061458 Solanum melongena Species 0.000 claims description 2
- 235000002597 Solanum melongena Nutrition 0.000 claims description 2
- 235000009337 Spinacia oleracea Nutrition 0.000 claims description 2
- 244000300264 Spinacia oleracea Species 0.000 claims description 2
- 102000002287 alpha Subunit Glycoprotein Hormones Human genes 0.000 claims description 2
- 108010000732 alpha Subunit Glycoprotein Hormones Proteins 0.000 claims description 2
- 230000002265 prevention Effects 0.000 claims description 2
- 102000018997 Growth Hormone Human genes 0.000 claims 1
- 108010034504 RC 101 Proteins 0.000 claims 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 1
- 239000003392 amylase inhibitor Substances 0.000 claims 1
- 238000012423 maintenance Methods 0.000 claims 1
- 239000000203 mixture Substances 0.000 abstract description 11
- 239000005090 green fluorescent protein Substances 0.000 description 196
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 170
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 170
- 235000018102 proteins Nutrition 0.000 description 110
- 102000009016 Cholera Toxin Human genes 0.000 description 49
- 108010049048 Cholera Toxin Proteins 0.000 description 49
- 210000000170 cell membrane Anatomy 0.000 description 36
- 239000003814 drug Substances 0.000 description 30
- 108091007433 antigens Proteins 0.000 description 29
- 102000036639 antigens Human genes 0.000 description 29
- 210000000805 cytoplasm Anatomy 0.000 description 29
- 239000000427 antigen Substances 0.000 description 27
- 102000004196 processed proteins & peptides Human genes 0.000 description 23
- 102000005962 receptors Human genes 0.000 description 22
- 108020003175 receptors Proteins 0.000 description 22
- 229940079593 drug Drugs 0.000 description 21
- 108020004414 DNA Proteins 0.000 description 19
- 210000003763 chloroplast Anatomy 0.000 description 19
- 241000699670 Mus sp. Species 0.000 description 16
- 239000000463 material Substances 0.000 description 16
- 210000004185 liver Anatomy 0.000 description 15
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 14
- 210000002919 epithelial cell Anatomy 0.000 description 14
- 230000000968 intestinal effect Effects 0.000 description 14
- 235000001014 amino acid Nutrition 0.000 description 13
- 210000002540 macrophage Anatomy 0.000 description 13
- 102000040430 polynucleotide Human genes 0.000 description 13
- 108091033319 polynucleotide Proteins 0.000 description 13
- 239000002157 polynucleotide Substances 0.000 description 13
- 210000002966 serum Anatomy 0.000 description 13
- 125000003275 alpha amino acid group Chemical group 0.000 description 12
- 210000005260 human cell Anatomy 0.000 description 12
- 210000000987 immune system Anatomy 0.000 description 12
- 210000000936 intestine Anatomy 0.000 description 12
- 238000009825 accumulation Methods 0.000 description 11
- 101150075980 psbA gene Proteins 0.000 description 11
- FWBHETKCLVMNFS-UHFFFAOYSA-N 4',6-Diamino-2-phenylindol Chemical compound C1=CC(C(=N)N)=CC=C1C1=CC2=CC=C(C(N)=N)C=C2N1 FWBHETKCLVMNFS-UHFFFAOYSA-N 0.000 description 10
- 210000001744 T-lymphocyte Anatomy 0.000 description 10
- 229940024606 amino acid Drugs 0.000 description 10
- 150000001413 amino acids Chemical class 0.000 description 10
- 230000006698 induction Effects 0.000 description 10
- 210000002490 intestinal epithelial cell Anatomy 0.000 description 10
- 229920001184 polypeptide Polymers 0.000 description 10
- 210000000844 retinal pigment epithelial cell Anatomy 0.000 description 10
- 238000010361 transduction Methods 0.000 description 10
- 230000026683 transduction Effects 0.000 description 10
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 9
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 9
- 210000002421 cell wall Anatomy 0.000 description 9
- 230000000694 effects Effects 0.000 description 9
- 210000003630 histaminocyte Anatomy 0.000 description 9
- 230000004957 immunoregulator effect Effects 0.000 description 9
- 238000000338 in vitro Methods 0.000 description 9
- 238000011534 incubation Methods 0.000 description 9
- 230000003993 interaction Effects 0.000 description 9
- 210000002901 mesenchymal stem cell Anatomy 0.000 description 9
- 238000000746 purification Methods 0.000 description 9
- 210000000130 stem cell Anatomy 0.000 description 9
- 230000009466 transformation Effects 0.000 description 9
- 239000013598 vector Substances 0.000 description 9
- 108091026890 Coding region Proteins 0.000 description 8
- 102000053602 DNA Human genes 0.000 description 8
- 210000003719 b-lymphocyte Anatomy 0.000 description 8
- 210000004369 blood Anatomy 0.000 description 8
- 239000008280 blood Substances 0.000 description 8
- 239000012634 fragment Substances 0.000 description 8
- 230000006870 function Effects 0.000 description 8
- 230000004807 localization Effects 0.000 description 8
- 230000001105 regulatory effect Effects 0.000 description 8
- 230000008685 targeting Effects 0.000 description 8
- 230000032258 transport Effects 0.000 description 8
- 108091034117 Oligonucleotide Proteins 0.000 description 7
- 238000003556 assay Methods 0.000 description 7
- 230000027455 binding Effects 0.000 description 7
- 230000000295 complement effect Effects 0.000 description 7
- 238000004108 freeze drying Methods 0.000 description 7
- 230000001965 increasing effect Effects 0.000 description 7
- 239000000523 sample Substances 0.000 description 7
- 238000006467 substitution reaction Methods 0.000 description 7
- 241001465754 Metazoa Species 0.000 description 6
- 230000008859 change Effects 0.000 description 6
- 239000000284 extract Substances 0.000 description 6
- 238000009396 hybridization Methods 0.000 description 6
- 230000028993 immune response Effects 0.000 description 6
- 210000003292 kidney cell Anatomy 0.000 description 6
- 230000034701 macropinocytosis Effects 0.000 description 6
- 230000007246 mechanism Effects 0.000 description 6
- 238000012385 systemic delivery Methods 0.000 description 6
- 230000020192 tolerance induction in gut-associated lymphoid tissue Effects 0.000 description 6
- 108010051109 Cell-Penetrating Peptides Proteins 0.000 description 5
- 102000020313 Cell-Penetrating Peptides Human genes 0.000 description 5
- 238000002965 ELISA Methods 0.000 description 5
- 108060003951 Immunoglobulin Proteins 0.000 description 5
- 241000699666 Mus <mouse, genus> Species 0.000 description 5
- 229930040373 Paraformaldehyde Natural products 0.000 description 5
- 102000035195 Peptidases Human genes 0.000 description 5
- 239000004365 Protease Substances 0.000 description 5
- 108700019146 Transgenes Proteins 0.000 description 5
- 238000013459 approach Methods 0.000 description 5
- 230000001413 cellular effect Effects 0.000 description 5
- KAFGYXORACVKTE-UEDJBKKJSA-N chembl503567 Chemical compound C([C@H]1C(=O)N[C@H]2CSSC[C@H](NC(=O)[C@H](CC=3C=CC=CC=3)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@H](C(=O)N[C@@H](CSSC[C@@H](C(N1)=O)NC(=O)[C@@H](NC(=O)[C@H](CCCNC(N)=N)NC(=O)CNC(=O)CNC(=O)[C@@H](N)CCCNC(N)=N)CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)C1=CC=C(O)C=C1 KAFGYXORACVKTE-UEDJBKKJSA-N 0.000 description 5
- 239000000499 gel Substances 0.000 description 5
- 102000018358 immunoglobulin Human genes 0.000 description 5
- 210000004347 intestinal mucosa Anatomy 0.000 description 5
- 210000004379 membrane Anatomy 0.000 description 5
- 239000012528 membrane Substances 0.000 description 5
- 244000005700 microbiome Species 0.000 description 5
- 239000000178 monomer Substances 0.000 description 5
- 210000000056 organ Anatomy 0.000 description 5
- 229920002866 paraformaldehyde Polymers 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 5
- 238000010186 staining Methods 0.000 description 5
- 238000005406 washing Methods 0.000 description 5
- 108020004635 Complementary DNA Proteins 0.000 description 4
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 4
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 4
- 108091006052 GFP-tagged proteins Proteins 0.000 description 4
- 108700008625 Reporter Genes Proteins 0.000 description 4
- 238000002105 Southern blotting Methods 0.000 description 4
- 229930006000 Sucrose Natural products 0.000 description 4
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 4
- 238000010804 cDNA synthesis Methods 0.000 description 4
- 239000002299 complementary DNA Substances 0.000 description 4
- 230000001086 cytosolic effect Effects 0.000 description 4
- 238000000326 densiometry Methods 0.000 description 4
- 210000002249 digestive system Anatomy 0.000 description 4
- 238000012377 drug delivery Methods 0.000 description 4
- 239000011536 extraction buffer Substances 0.000 description 4
- 210000003128 head Anatomy 0.000 description 4
- 229940088597 hormone Drugs 0.000 description 4
- 239000005556 hormone Substances 0.000 description 4
- 230000002209 hydrophobic effect Effects 0.000 description 4
- 238000003780 insertion Methods 0.000 description 4
- 230000037431 insertion Effects 0.000 description 4
- 210000001165 lymph node Anatomy 0.000 description 4
- 239000002773 nucleotide Substances 0.000 description 4
- 125000003729 nucleotide group Chemical group 0.000 description 4
- 210000000963 osteoblast Anatomy 0.000 description 4
- 210000002379 periodontal ligament Anatomy 0.000 description 4
- 230000008569 process Effects 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 238000011002 quantification Methods 0.000 description 4
- 210000000813 small intestine Anatomy 0.000 description 4
- 210000002536 stromal cell Anatomy 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 239000005720 sucrose Substances 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- 238000012546 transfer Methods 0.000 description 4
- 238000001262 western blot Methods 0.000 description 4
- CFBILACNYSPRPM-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;2-[[1,3-dihydroxy-2-(hydroxymethyl)propan-2-yl]amino]acetic acid Chemical compound OCC(N)(CO)CO.OCC(CO)(CO)NCC(O)=O CFBILACNYSPRPM-UHFFFAOYSA-N 0.000 description 3
- 108020003589 5' Untranslated Regions Proteins 0.000 description 3
- 239000012103 Alexa Fluor 488 Substances 0.000 description 3
- 102000004127 Cytokines Human genes 0.000 description 3
- 108090000695 Cytokines Proteins 0.000 description 3
- 241000283074 Equus asinus Species 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 241000283973 Oryctolagus cuniculus Species 0.000 description 3
- 206010061902 Pancreatic neoplasm Diseases 0.000 description 3
- 102100038803 Somatotropin Human genes 0.000 description 3
- 230000004913 activation Effects 0.000 description 3
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical class N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 3
- 238000010171 animal model Methods 0.000 description 3
- 210000000612 antigen-presenting cell Anatomy 0.000 description 3
- 229960000074 biopharmaceutical Drugs 0.000 description 3
- 210000004556 brain Anatomy 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 150000001720 carbohydrates Chemical class 0.000 description 3
- 235000014633 carbohydrates Nutrition 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 238000004624 confocal microscopy Methods 0.000 description 3
- 230000002950 deficient Effects 0.000 description 3
- 238000009826 distribution Methods 0.000 description 3
- 230000012202 endocytosis Effects 0.000 description 3
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 3
- 239000003623 enhancer Substances 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 235000011389 fruit/vegetable juice Nutrition 0.000 description 3
- 210000001035 gastrointestinal tract Anatomy 0.000 description 3
- 238000003384 imaging method Methods 0.000 description 3
- 238000003119 immunoblot Methods 0.000 description 3
- 238000010348 incorporation Methods 0.000 description 3
- 230000010354 integration Effects 0.000 description 3
- 210000003734 kidney Anatomy 0.000 description 3
- 239000003446 ligand Substances 0.000 description 3
- 210000004072 lung Anatomy 0.000 description 3
- 210000004698 lymphocyte Anatomy 0.000 description 3
- 208000015486 malignant pancreatic neoplasm Diseases 0.000 description 3
- 210000004962 mammalian cell Anatomy 0.000 description 3
- 230000001404 mediated effect Effects 0.000 description 3
- 239000013642 negative control Substances 0.000 description 3
- 201000002528 pancreatic cancer Diseases 0.000 description 3
- 208000008443 pancreatic carcinoma Diseases 0.000 description 3
- 210000000277 pancreatic duct Anatomy 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 230000017854 proteolysis Effects 0.000 description 3
- 238000005057 refrigeration Methods 0.000 description 3
- 210000003289 regulatory T cell Anatomy 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 238000012216 screening Methods 0.000 description 3
- 238000003860 storage Methods 0.000 description 3
- 238000013519 translation Methods 0.000 description 3
- 229960005486 vaccine Drugs 0.000 description 3
- 239000003981 vehicle Substances 0.000 description 3
- 230000029663 wound healing Effects 0.000 description 3
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 2
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 2
- 108020005345 3' Untranslated Regions Proteins 0.000 description 2
- 239000004382 Amylase Substances 0.000 description 2
- 239000004475 Arginine Substances 0.000 description 2
- 208000023275 Autoimmune disease Diseases 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 108010039209 Blood Coagulation Factors Proteins 0.000 description 2
- 102000015081 Blood Coagulation Factors Human genes 0.000 description 2
- 238000009010 Bradford assay Methods 0.000 description 2
- VTYYLEPIZMXCLO-UHFFFAOYSA-L Calcium carbonate Chemical compound [Ca+2].[O-]C([O-])=O VTYYLEPIZMXCLO-UHFFFAOYSA-L 0.000 description 2
- 108010078791 Carrier Proteins Proteins 0.000 description 2
- 238000012286 ELISA Assay Methods 0.000 description 2
- 208000005189 Embolism Diseases 0.000 description 2
- 108010011459 Exenatide Proteins 0.000 description 2
- 102000003972 Fibroblast growth factor 7 Human genes 0.000 description 2
- 108090000385 Fibroblast growth factor 7 Proteins 0.000 description 2
- 102000004961 Furin Human genes 0.000 description 2
- 108090001126 Furin Proteins 0.000 description 2
- 108091092584 GDNA Proteins 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 108010070875 Human Immunodeficiency Virus tat Gene Products Proteins 0.000 description 2
- 206010020751 Hypersensitivity Diseases 0.000 description 2
- 206010020772 Hypertension Diseases 0.000 description 2
- 102000003814 Interleukin-10 Human genes 0.000 description 2
- 108090000174 Interleukin-10 Proteins 0.000 description 2
- LRHPLDYGYMQRHN-UHFFFAOYSA-N N-Butanol Chemical compound CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 241000208134 Nicotiana rustica Species 0.000 description 2
- 108091028043 Nucleic acid sequence Proteins 0.000 description 2
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 2
- 101710183548 Pyridoxal 5'-phosphate synthase subunit PdxS Proteins 0.000 description 2
- 102100035459 Pyruvate dehydrogenase protein X component, mitochondrial Human genes 0.000 description 2
- 108020004682 Single-Stranded DNA Proteins 0.000 description 2
- 208000000102 Squamous Cell Carcinoma of Head and Neck Diseases 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 208000026935 allergic disease Diseases 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 2
- 235000011130 ammonium sulphate Nutrition 0.000 description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 2
- 230000004888 barrier function Effects 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 210000004899 c-terminal region Anatomy 0.000 description 2
- 238000004364 calculation method Methods 0.000 description 2
- 239000002775 capsule Substances 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 230000015861 cell surface binding Effects 0.000 description 2
- 230000004700 cellular uptake Effects 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 238000002512 chemotherapy Methods 0.000 description 2
- 238000002983 circular dichroism Methods 0.000 description 2
- 238000004590 computer program Methods 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 238000002716 delivery method Methods 0.000 description 2
- 238000011033 desalting Methods 0.000 description 2
- 206010012601 diabetes mellitus Diseases 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 235000018927 edible plant Nutrition 0.000 description 2
- 238000005538 encapsulation Methods 0.000 description 2
- 229960001519 exenatide Drugs 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 230000037406 food intake Effects 0.000 description 2
- QPJBWNIQKHGLAU-IQZHVAEDSA-N ganglioside GM1 Chemical compound O[C@@H]1[C@@H](O)[C@H](OC[C@H](NC(=O)CCCCCCCCCCCCCCCCC)[C@H](O)\C=C\CCCCCCCCCCCCC)O[C@H](CO)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@]2(O[C@H]([C@H](NC(C)=O)[C@@H](O)C2)[C@H](O)[C@H](O)CO)C(O)=O)[C@@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O3)O)[C@@H](O)[C@@H](CO)O2)NC(C)=O)[C@@H](CO)O1 QPJBWNIQKHGLAU-IQZHVAEDSA-N 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 210000004195 gingiva Anatomy 0.000 description 2
- 239000008187 granular material Substances 0.000 description 2
- 210000004837 gut-associated lymphoid tissue Anatomy 0.000 description 2
- 201000000459 head and neck squamous cell carcinoma Diseases 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 230000013632 homeostatic process Effects 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 239000001257 hydrogen Substances 0.000 description 2
- 210000003405 ileum Anatomy 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 230000006058 immune tolerance Effects 0.000 description 2
- 238000003125 immunofluorescent labeling Methods 0.000 description 2
- 230000001506 immunosuppresive effect Effects 0.000 description 2
- 238000009169 immunotherapy Methods 0.000 description 2
- 230000001939 inductive effect Effects 0.000 description 2
- 208000015181 infectious disease Diseases 0.000 description 2
- 230000000977 initiatory effect Effects 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 230000002452 interceptive effect Effects 0.000 description 2
- 238000002372 labelling Methods 0.000 description 2
- 229920002521 macromolecule Polymers 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 108020004999 messenger RNA Proteins 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 231100000252 nontoxic Toxicity 0.000 description 2
- 230000003000 nontoxic effect Effects 0.000 description 2
- 230000030648 nucleus localization Effects 0.000 description 2
- 238000003305 oral gavage Methods 0.000 description 2
- 239000012074 organic phase Substances 0.000 description 2
- 230000037361 pathway Effects 0.000 description 2
- 239000008188 pellet Substances 0.000 description 2
- 201000001245 periodontitis Diseases 0.000 description 2
- 210000001986 peyer's patch Anatomy 0.000 description 2
- 238000002823 phage display Methods 0.000 description 2
- 239000000546 pharmaceutical excipient Substances 0.000 description 2
- 239000012071 phase Substances 0.000 description 2
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 2
- 239000000419 plant extract Substances 0.000 description 2
- 239000013600 plasmid vector Substances 0.000 description 2
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 2
- 210000003240 portal vein Anatomy 0.000 description 2
- 230000001323 posttranslational effect Effects 0.000 description 2
- 108010032968 protegrin-4 Proteins 0.000 description 2
- DUDXZJRHGONAAZ-ZFOLPASKSA-N protegrin-4 Chemical compound C([C@@H]1NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)CNC(=O)CNC(=O)[C@@H](N)CCCNC(N)=N)CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@@H]2CSSC[C@H](NC1=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C3=CC=CC=C3NC=1)C(=O)N[C@H](C(N2)=O)[C@@H](C)CC)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(N)=O)C1=CC=C(O)C=C1 DUDXZJRHGONAAZ-ZFOLPASKSA-N 0.000 description 2
- 238000000159 protein binding assay Methods 0.000 description 2
- 238000001742 protein purification Methods 0.000 description 2
- 230000006337 proteolytic cleavage Effects 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 230000002207 retinal effect Effects 0.000 description 2
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 230000009885 systemic effect Effects 0.000 description 2
- 229940126585 therapeutic drug Drugs 0.000 description 2
- 238000002560 therapeutic procedure Methods 0.000 description 2
- 230000024664 tolerance induction Effects 0.000 description 2
- 210000003412 trans-golgi network Anatomy 0.000 description 2
- 238000013518 transcription Methods 0.000 description 2
- 230000035897 transcription Effects 0.000 description 2
- 230000031998 transcytosis Effects 0.000 description 2
- 239000004474 valine Substances 0.000 description 2
- 239000013603 viral vector Substances 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- PXFBZOLANLWPMH-UHFFFAOYSA-N 16-Epiaffinine Natural products C1C(C2=CC=CC=C2N2)=C2C(=O)CC2C(=CC)CN(C)C1C2CO PXFBZOLANLWPMH-UHFFFAOYSA-N 0.000 description 1
- BUOYTFVLNZIELF-UHFFFAOYSA-N 2-phenyl-1h-indole-4,6-dicarboximidamide Chemical compound N1C2=CC(C(=N)N)=CC(C(N)=N)=C2C=C1C1=CC=CC=C1 BUOYTFVLNZIELF-UHFFFAOYSA-N 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 101710186708 Agglutinin Proteins 0.000 description 1
- 241000589158 Agrobacterium Species 0.000 description 1
- 108010058060 Alanine-tRNA ligase Proteins 0.000 description 1
- 102100037399 Alanine-tRNA ligase, cytoplasmic Human genes 0.000 description 1
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
- 206010002198 Anaphylactic reaction Diseases 0.000 description 1
- 101710081722 Antitrypsin Proteins 0.000 description 1
- 102000015790 Asparaginase Human genes 0.000 description 1
- 108010024976 Asparaginase Proteins 0.000 description 1
- 108091008875 B cell receptors Proteins 0.000 description 1
- 239000002028 Biomass Substances 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 108030001720 Bontoxilysin Proteins 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 102000005367 Carboxypeptidases Human genes 0.000 description 1
- 108010006303 Carboxypeptidases Proteins 0.000 description 1
- 201000009030 Carcinoma Diseases 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 241000122205 Chamaeleonidae Species 0.000 description 1
- 108700031407 Chloroplast Genes Proteins 0.000 description 1
- 206010008631 Cholera Diseases 0.000 description 1
- 102000011022 Chorionic Gonadotropin Human genes 0.000 description 1
- 108010062540 Chorionic Gonadotropin Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 102000029816 Collagenase Human genes 0.000 description 1
- 108060005980 Collagenase Proteins 0.000 description 1
- 201000003883 Cystic fibrosis Diseases 0.000 description 1
- 208000018035 Dental disease Diseases 0.000 description 1
- 102000016911 Deoxyribonucleases Human genes 0.000 description 1
- 108010053770 Deoxyribonucleases Proteins 0.000 description 1
- 208000012239 Developmental disease Diseases 0.000 description 1
- 208000030453 Drug-Related Side Effects and Adverse reaction Diseases 0.000 description 1
- 208000014094 Dystonic disease Diseases 0.000 description 1
- 238000008157 ELISA kit Methods 0.000 description 1
- 108010067770 Endopeptidase K Proteins 0.000 description 1
- HTQBXNHDCUEHJF-XWLPCZSASA-N Exenatide Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(=O)NCC(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CO)C(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)[C@@H](C)O)C(C)C)C1=CC=CC=C1 HTQBXNHDCUEHJF-XWLPCZSASA-N 0.000 description 1
- 230000010682 Fusion Protein Interactions Effects 0.000 description 1
- 208000018522 Gastrointestinal disease Diseases 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 108700028146 Genetic Enhancer Elements Proteins 0.000 description 1
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 208000031220 Hemophilia Diseases 0.000 description 1
- 208000009292 Hemophilia A Diseases 0.000 description 1
- 208000005176 Hepatitis C Diseases 0.000 description 1
- 102000007625 Hirudins Human genes 0.000 description 1
- 108010007267 Hirudins Proteins 0.000 description 1
- 101000929495 Homo sapiens Adenosine deaminase Proteins 0.000 description 1
- 101710146024 Horcolin Proteins 0.000 description 1
- 208000026350 Inborn Genetic disease Diseases 0.000 description 1
- 102100022297 Integrin alpha-X Human genes 0.000 description 1
- 102000006992 Interferon-alpha Human genes 0.000 description 1
- 108010047761 Interferon-alpha Proteins 0.000 description 1
- 102000003996 Interferon-beta Human genes 0.000 description 1
- 108090000467 Interferon-beta Proteins 0.000 description 1
- 102000029793 Isoleucine-tRNA ligase Human genes 0.000 description 1
- 101710176147 Isoleucine-tRNA ligase, cytoplasmic Proteins 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 108091026898 Leader sequence (mRNA) Proteins 0.000 description 1
- 101710138460 Leaf protein Proteins 0.000 description 1
- 101710189395 Lectin Proteins 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 208000019693 Lung disease Diseases 0.000 description 1
- 102000008072 Lymphokines Human genes 0.000 description 1
- 108010074338 Lymphokines Proteins 0.000 description 1
- 208000015439 Lysosomal storage disease Diseases 0.000 description 1
- 102000043129 MHC class I family Human genes 0.000 description 1
- 108091054437 MHC class I family Proteins 0.000 description 1
- 102000043131 MHC class II family Human genes 0.000 description 1
- 108091054438 MHC class II family Proteins 0.000 description 1
- 244000141359 Malus pumila Species 0.000 description 1
- 101710179758 Mannose-specific lectin Proteins 0.000 description 1
- 101710150763 Mannose-specific lectin 1 Proteins 0.000 description 1
- 101710150745 Mannose-specific lectin 2 Proteins 0.000 description 1
- 229910014130 Na—P Inorganic materials 0.000 description 1
- 206010029164 Nephrotic syndrome Diseases 0.000 description 1
- 206010033645 Pancreatitis Diseases 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 108090000445 Parathyroid hormone Proteins 0.000 description 1
- 102000003982 Parathyroid hormone Human genes 0.000 description 1
- 108700020962 Peroxidase Proteins 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 102000010780 Platelet-Derived Growth Factor Human genes 0.000 description 1
- 108010038512 Platelet-Derived Growth Factor Proteins 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 101710149031 Probable isoleucine-tRNA ligase, cytoplasmic Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 108010059712 Pronase Proteins 0.000 description 1
- 101800004937 Protein C Proteins 0.000 description 1
- 108010029485 Protein Isoforms Proteins 0.000 description 1
- 102000001708 Protein Isoforms Human genes 0.000 description 1
- 239000012083 RIPA buffer Substances 0.000 description 1
- 101710146873 Receptor-binding protein Proteins 0.000 description 1
- 208000017442 Retinal disease Diseases 0.000 description 1
- 206010038923 Retinopathy Diseases 0.000 description 1
- 108091028664 Ribonucleotide Proteins 0.000 description 1
- 108010003581 Ribulose-bisphosphate carboxylase Proteins 0.000 description 1
- 101800001700 Saposin-D Proteins 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 108010023197 Streptokinase Proteins 0.000 description 1
- 238000000692 Student's t-test Methods 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 210000004241 Th2 cell Anatomy 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 206010070863 Toxicity to various agents Diseases 0.000 description 1
- 102000004887 Transforming Growth Factor beta Human genes 0.000 description 1
- 108090001012 Transforming Growth Factor beta Proteins 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 208000025865 Ulcer Diseases 0.000 description 1
- 240000003864 Ulex europaeus Species 0.000 description 1
- 235000010730 Ulex europaeus Nutrition 0.000 description 1
- 206010047249 Venous thrombosis Diseases 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 230000033289 adaptive immune response Effects 0.000 description 1
- 230000004721 adaptive immunity Effects 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 238000000246 agarose gel electrophoresis Methods 0.000 description 1
- 239000000910 agglutinin Substances 0.000 description 1
- 230000007815 allergy Effects 0.000 description 1
- 229940126575 aminoglycoside Drugs 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 230000036783 anaphylactic response Effects 0.000 description 1
- 208000003455 anaphylaxis Diseases 0.000 description 1
- 208000007502 anemia Diseases 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 230000003110 anti-inflammatory effect Effects 0.000 description 1
- 230000002223 anti-pathogen Effects 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- 230000001475 anti-trypsic effect Effects 0.000 description 1
- 230000002155 anti-virotic effect Effects 0.000 description 1
- 230000030741 antigen processing and presentation Effects 0.000 description 1
- 235000021016 apples Nutrition 0.000 description 1
- 239000008346 aqueous phase Substances 0.000 description 1
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 1
- 229960003272 asparaginase Drugs 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-M asparaginate Chemical compound [O-]C(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-M 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N aspartic acid group Chemical class N[C@@H](CC(=O)O)C(=O)O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- 230000005784 autoimmunity Effects 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000008236 biological pathway Effects 0.000 description 1
- 229940019700 blood coagulation factors Drugs 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 229940053031 botulinum toxin Drugs 0.000 description 1
- 125000000484 butyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 229910000019 calcium carbonate Inorganic materials 0.000 description 1
- 238000004422 calculation algorithm Methods 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 238000002619 cancer immunotherapy Methods 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000004709 cell invasion Effects 0.000 description 1
- 230000007969 cellular immunity Effects 0.000 description 1
- 230000036755 cellular response Effects 0.000 description 1
- 235000013339 cereals Nutrition 0.000 description 1
- JUFFVKRROAPVBI-PVOYSMBESA-N chembl1210015 Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(=O)N[C@H]1[C@@H]([C@@H](O)[C@H](O[C@H]2[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO[C@]3(O[C@@H](C[C@H](O)[C@H](O)CO)[C@H](NC(C)=O)[C@@H](O)C3)C(O)=O)O2)O)[C@@H](CO)O1)NC(C)=O)C(=O)NCC(=O)NCC(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CO)C(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)[C@@H](C)O)C(C)C)C1=CC=CC=C1 JUFFVKRROAPVBI-PVOYSMBESA-N 0.000 description 1
- 229940015047 chorionic gonadotropin Drugs 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 208000037976 chronic inflammation Diseases 0.000 description 1
- 230000006020 chronic inflammation Effects 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 230000008045 co-localization Effects 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 229960002424 collagenase Drugs 0.000 description 1
- 238000010226 confocal imaging Methods 0.000 description 1
- 210000004351 coronary vessel Anatomy 0.000 description 1
- 239000002537 cosmetic Substances 0.000 description 1
- 238000002316 cosmetic surgery Methods 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 210000000172 cytosol Anatomy 0.000 description 1
- 230000007123 defense Effects 0.000 description 1
- 239000005547 deoxyribonucleotide Substances 0.000 description 1
- 125000002637 deoxyribonucleotide group Chemical group 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 102000038379 digestive enzymes Human genes 0.000 description 1
- 108091007734 digestive enzymes Proteins 0.000 description 1
- 208000010643 digestive system disease Diseases 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 230000009977 dual effect Effects 0.000 description 1
- 230000002183 duodenal effect Effects 0.000 description 1
- 208000010118 dystonia Diseases 0.000 description 1
- 235000013399 edible fruits Nutrition 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 210000003038 endothelium Anatomy 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 210000000981 epithelium Anatomy 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 230000035558 fertility Effects 0.000 description 1
- 238000002073 fluorescence micrograph Methods 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 235000012041 food component Nutrition 0.000 description 1
- 239000005417 food ingredient Substances 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 210000004211 gastric acid Anatomy 0.000 description 1
- 208000018685 gastrointestinal system disease Diseases 0.000 description 1
- 238000003304 gavage Methods 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 230000009368 gene silencing by RNA Effects 0.000 description 1
- 208000016361 genetic disease Diseases 0.000 description 1
- 230000035784 germination Effects 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 210000003714 granulocyte Anatomy 0.000 description 1
- 235000021384 green leafy vegetables Nutrition 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 210000003958 hematopoietic stem cell Anatomy 0.000 description 1
- 230000011132 hemopoiesis Effects 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- WQPDUTSPKFMPDP-OUMQNGNKSA-N hirudin Chemical compound C([C@@H](C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C=CC(OS(O)(=O)=O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCCN)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H]1NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@@H]2CSSC[C@@H](C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@H](C(NCC(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N2)=O)CSSC1)C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=2C=CC(O)=CC=2)NC(=O)[C@@H](NC(=O)[C@@H](N)C(C)C)C(C)C)[C@@H](C)O)CSSC1)C(C)C)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 WQPDUTSPKFMPDP-OUMQNGNKSA-N 0.000 description 1
- 229940006607 hirudin Drugs 0.000 description 1
- 102000043395 human ADA Human genes 0.000 description 1
- 230000004727 humoral immunity Effects 0.000 description 1
- 125000002883 imidazolyl group Chemical group 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 230000002055 immunohistochemical effect Effects 0.000 description 1
- 238000003364 immunohistochemistry Methods 0.000 description 1
- 238000012744 immunostaining Methods 0.000 description 1
- 230000028709 inflammatory response Effects 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000015788 innate immune response Effects 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 206010022498 insulinoma Diseases 0.000 description 1
- 229960001388 interferon-beta Drugs 0.000 description 1
- 229940047124 interferons Drugs 0.000 description 1
- 230000006917 intersubunit interaction Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 230000009545 invasion Effects 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 210000004153 islets of langerhan Anatomy 0.000 description 1
- 238000001155 isoelectric focusing Methods 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 125000001909 leucine group Chemical class [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 208000032839 leukemia Diseases 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 210000005229 liver cell Anatomy 0.000 description 1
- 210000005228 liver tissue Anatomy 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 238000012792 lyophilization process Methods 0.000 description 1
- 239000008176 lyophilized powder Substances 0.000 description 1
- 210000003126 m-cell Anatomy 0.000 description 1
- 210000002050 maxilla Anatomy 0.000 description 1
- 102000006240 membrane receptors Human genes 0.000 description 1
- 108020004084 membrane receptors Proteins 0.000 description 1
- 230000037353 metabolic pathway Effects 0.000 description 1
- 238000000520 microinjection Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 230000001617 migratory effect Effects 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- 210000004400 mucous membrane Anatomy 0.000 description 1
- 201000006417 multiple sclerosis Diseases 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 210000000066 myeloid cell Anatomy 0.000 description 1
- 210000000653 nervous system Anatomy 0.000 description 1
- 238000012758 nuclear staining Methods 0.000 description 1
- 229920002113 octoxynol Polymers 0.000 description 1
- 239000006179 pH buffering agent Substances 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 208000021255 pancreatic insulinoma Diseases 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 239000000199 parathyroid hormone Substances 0.000 description 1
- 229960001319 parathyroid hormone Drugs 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 230000007903 penetration ability Effects 0.000 description 1
- 230000003239 periodontal effect Effects 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 150000003904 phospholipids Chemical class 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- WVMOUHNEDGUTQU-GPOLKXGASA-N protegrin 2 Chemical compound C([C@H]1C(=O)N[C@H]2CSSC[C@H](NC(=O)[C@H](CC=3C=CC=CC=3)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@H](C(N[C@@H](CSSC[C@@H](C(=O)N1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)CNC(=O)CNC(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](C(C)C)C(N)=O)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 WVMOUHNEDGUTQU-GPOLKXGASA-N 0.000 description 1
- KZAZIWVZJLUFCN-DPAFCJMGSA-N protegrin 3 Chemical compound C([C@H]1C(=O)N[C@H]2CSSC[C@H](NC(=O)[C@H](CC=3C=CC=CC=3)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@H](C(=O)N[C@@H](CSSC[C@@H](C(N1)=O)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)CNC(=O)[C@@H](N)CCCNC(N)=N)CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(N)=O)C(C)C)C1=CC=C(O)C=C1 KZAZIWVZJLUFCN-DPAFCJMGSA-N 0.000 description 1
- 108010032979 protegrin-2 Proteins 0.000 description 1
- 108010032978 protegrin-3 Proteins 0.000 description 1
- 108010032974 protegrin-5 Proteins 0.000 description 1
- JCKSZPLZVLHFMU-UEDJBKKJSA-N protegrin-5 Chemical compound C([C@H]1C(=O)N[C@H]2CSSC[C@H](NC(=O)[C@H](CC=3C=CC=CC=3)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@@H]3CCCN3C(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@H](C(=O)N[C@@H](CSSC[C@@H](C(N1)=O)NC(=O)[C@@H](NC(=O)[C@H](CCCNC(N)=N)NC(=O)CNC(=O)CNC(=O)[C@@H](N)CCCNC(N)=N)CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(N)=O)C(C)C)C1=CC=C(O)C=C1 JCKSZPLZVLHFMU-UEDJBKKJSA-N 0.000 description 1
- 238000000164 protein isolation Methods 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 description 1
- 239000003488 releasing hormone Substances 0.000 description 1
- 238000009256 replacement therapy Methods 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 230000003362 replicative effect Effects 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 210000001525 retina Anatomy 0.000 description 1
- 239000002336 ribonucleotide Substances 0.000 description 1
- 125000002652 ribonucleotide group Chemical group 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 238000013341 scale-up Methods 0.000 description 1
- 238000011896 sensitive detection Methods 0.000 description 1
- 239000000741 silica gel Substances 0.000 description 1
- 229910002027 silica gel Inorganic materials 0.000 description 1
- 210000002027 skeletal muscle Anatomy 0.000 description 1
- 229940126586 small molecule drug Drugs 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
- 230000000392 somatic effect Effects 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 125000006850 spacer group Chemical group 0.000 description 1
- 210000000278 spinal cord Anatomy 0.000 description 1
- 206010041823 squamous cell carcinoma Diseases 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 208000003265 stomatitis Diseases 0.000 description 1
- 229960005202 streptokinase Drugs 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 239000003826 tablet Substances 0.000 description 1
- ZRKFYGHZFMAOKI-QMGMOQQFSA-N tgfbeta Chemical compound C([C@H](NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O)C1=CC=C(O)C=C1 ZRKFYGHZFMAOKI-QMGMOQQFSA-N 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 150000003587 threonine derivatives Chemical class 0.000 description 1
- 230000003614 tolerogenic effect Effects 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 230000005030 transcription termination Effects 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 230000014621 translational initiation Effects 0.000 description 1
- 230000005945 translocation Effects 0.000 description 1
- 238000002054 transplantation Methods 0.000 description 1
- 239000002753 trypsin inhibitor Substances 0.000 description 1
- 230000037455 tumor specific immune response Effects 0.000 description 1
- 231100000397 ulcer Toxicity 0.000 description 1
- 238000009281 ultraviolet germicidal irradiation Methods 0.000 description 1
- 241001148471 unidentified anaerobic bacterium Species 0.000 description 1
- 239000002691 unilamellar liposome Substances 0.000 description 1
- 230000003827 upregulation Effects 0.000 description 1
- 125000002987 valine group Chemical group [H]N([H])C([H])(C(*)=O)C([H])(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 238000012800 visualization Methods 0.000 description 1
- 238000009736 wetting Methods 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/82—Vectors or expression systems specially adapted for eukaryotic hosts for plant cells, e.g. plant artificial chromosomes (PACs)
- C12N15/8241—Phenotypically and genetically modified plants via recombinant DNA technology
- C12N15/8242—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits
- C12N15/8257—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits for the production of primary gene products, e.g. pharmaceutical products, interferon
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K36/00—Medicinal preparations of undetermined constitution containing material from algae, lichens, fungi or plants, or derivatives thereof, e.g. traditional herbal medicines
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/0012—Galenical forms characterised by the site of application
- A61K9/0053—Mouth and digestive tract, i.e. intraoral and peroral administration
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/48—Preparations in capsules, e.g. of gelatin, of chocolate
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/28—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Vibrionaceae (F)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4723—Cationic antimicrobial peptides, e.g. defensins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/70596—Molecules with a "CD"-designation not provided for elsewhere
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/71—Receptors; Cell surface antigens; Cell surface determinants for growth factors; for growth regulators
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/82—Vectors or expression systems specially adapted for eukaryotic hosts for plant cells, e.g. plant artificial chromosomes (PACs)
- C12N15/8241—Phenotypically and genetically modified plants via recombinant DNA technology
- C12N15/8242—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits
- C12N15/8257—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits for the production of primary gene products, e.g. pharmaceutical products, interferon
- C12N15/8258—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits for the production of primary gene products, e.g. pharmaceutical products, interferon for the production of oral vaccines (antigens) or immunoglobulins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/60—Fusion polypeptide containing spectroscopic/fluorescent detection, e.g. green fluorescent protein [GFP]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/80—Fusion polypeptide containing a DNA binding domain, e.g. Lacl or Tet-repressor
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Biotechnology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Cell Biology (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Pharmacology & Pharmacy (AREA)
- Wood Science & Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Toxicology (AREA)
- Immunology (AREA)
- Microbiology (AREA)
- Animal Behavior & Ethology (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Epidemiology (AREA)
- Diabetes (AREA)
- Medical Informatics (AREA)
- Alternative & Traditional Medicine (AREA)
- Physiology (AREA)
- Nutrition Science (AREA)
- Natural Medicines & Medicinal Plants (AREA)
- Mycology (AREA)
- Botany (AREA)
- Hematology (AREA)
- Endocrinology (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201562256053P | 2015-11-16 | 2015-11-16 | |
| US62/256,053 | 2015-11-16 | ||
| PCT/US2016/062371 WO2017087582A1 (en) | 2015-11-16 | 2016-11-16 | Targeted delivery of therapeutic proteins bioencapsulated in plant cells to cell types of interest for the treatment of disease |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2019503341A true JP2019503341A (ja) | 2019-02-07 |
| JP2019503341A5 JP2019503341A5 (es) | 2019-12-26 |
Family
ID=58717784
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2018525435A Pending JP2019503341A (ja) | 2015-11-16 | 2016-11-16 | 植物細胞に生物学的に封入された、治療用タンパク質の、疾患の治療のための関心のある細胞型への標的化された送達 |
Country Status (7)
| Country | Link |
|---|---|
| US (1) | US20180327768A1 (es) |
| EP (1) | EP3377622A4 (es) |
| JP (1) | JP2019503341A (es) |
| CN (1) | CN108699548A (es) |
| AU (1) | AU2016355563A1 (es) |
| CA (1) | CA3043995A1 (es) |
| WO (1) | WO2017087582A1 (es) |
Families Citing this family (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN109385443B (zh) * | 2017-08-07 | 2022-08-02 | 北京睿诚海汇健康科技有限公司 | 生菜作为宿主在表达凝血因子中的应用 |
| CN110004180B (zh) * | 2019-04-16 | 2023-08-18 | 上海海洋大学 | 一种由功能肽a25修饰的基因载体及其制备方法和应用 |
| CN110256578B (zh) * | 2019-06-24 | 2021-04-23 | 王跃驹 | 植物生产人霍乱毒素b亚基(ctb)与胰岛素原的融合蛋白速效口服降糖胶囊的应用 |
| CN110272885A (zh) * | 2019-07-05 | 2019-09-24 | 王跃驹 | 植物源纳豆激酶胶囊及其生产方法 |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2015073988A1 (en) * | 2013-11-15 | 2015-05-21 | Trustees Of The University Of Pennsylvania | Compositions and methods for suppression of inhibitor formation against factor viii in hemophilia a patients |
Family Cites Families (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2004005467A2 (en) | 2002-07-03 | 2004-01-15 | University Of Central Florida | Expression of human interferon in transgenic chloroplasts |
| EP2080803B1 (en) | 2000-03-01 | 2011-05-25 | Auburn University | Plastid transformation vectors for expressing proinsulin fused to the cholera toxin B-subunit in plants |
| WO2001064023A1 (en) | 2000-03-02 | 2001-09-07 | Auburn University | Marker free transgenic plants: engineering the chloroplast genome without the use of antibiotic selection |
| WO2003057834A2 (en) | 2001-12-26 | 2003-07-17 | University Of Central Florida | Expression of protective antigens in transgenic chloroplasts and the production of improved vaccines |
| AU2003232081B2 (en) * | 2002-07-03 | 2009-02-05 | Brandeis University | Central airway administration for systemic delivery of therapeutics |
| EP2261364A3 (en) * | 2005-05-27 | 2011-03-30 | The University of Central Florida, | Chloroplasts engineered to express pharmaceutical proteins |
| AU2008232543B2 (en) * | 2007-03-30 | 2013-01-17 | University Of Central Florida Research Foundation, Inc. | Chloroplasts engineered to express pharmaceutical proteins in edible plants |
| GB2465749B (en) * | 2008-11-25 | 2013-05-08 | Algentech Sas | Plant cell transformation method |
| US20110091493A1 (en) * | 2009-10-16 | 2011-04-21 | Northwestern University | Vaccine compositions and uses thereof |
| EP2471929A1 (en) * | 2010-12-29 | 2012-07-04 | Algenics | Production of high mannose glycosylated proteins stored in the plastid of microalgae |
-
2016
- 2016-11-16 WO PCT/US2016/062371 patent/WO2017087582A1/en active Application Filing
- 2016-11-16 JP JP2018525435A patent/JP2019503341A/ja active Pending
- 2016-11-16 EP EP16867085.9A patent/EP3377622A4/en active Pending
- 2016-11-16 CN CN201680079066.1A patent/CN108699548A/zh active Pending
- 2016-11-16 CA CA3043995A patent/CA3043995A1/en active Pending
- 2016-11-16 AU AU2016355563A patent/AU2016355563A1/en not_active Abandoned
- 2016-11-16 US US15/776,602 patent/US20180327768A1/en not_active Abandoned
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2015073988A1 (en) * | 2013-11-15 | 2015-05-21 | Trustees Of The University Of Pennsylvania | Compositions and methods for suppression of inhibitor formation against factor viii in hemophilia a patients |
Also Published As
| Publication number | Publication date |
|---|---|
| CN108699548A (zh) | 2018-10-23 |
| EP3377622A4 (en) | 2019-06-19 |
| AU2016355563A1 (en) | 2018-06-21 |
| CA3043995A1 (en) | 2017-05-26 |
| US20180327768A1 (en) | 2018-11-15 |
| WO2017087582A1 (en) | 2017-05-26 |
| EP3377622A1 (en) | 2018-09-26 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Xiao et al. | Low cost delivery of proteins bioencapsulated in plant cells to human non-immune or immune modulatory cells | |
| US11358995B2 (en) | Compositions and methods of use for treating metabolic disorders | |
| Kwon et al. | Oral delivery of protein drugs bioencapsulated in plant cells | |
| CN103945861B (zh) | 胰高血糖素样肽-2组合物及其制备和使用方法 | |
| JP2021072853A (ja) | Ｘｔｅｎを有するトロンビン切断可能リンカー及びその使用 | |
| JP2019503341A (ja) | 植物細胞に生物学的に封入された、治療用タンパク質の、疾患の治療のための関心のある細胞型への標的化された送達 | |
| CA2428114A1 (en) | Apolipoprotein analogues | |
| CN101484469A (zh) | 生产胰岛素样生长因子-ⅰ的方法 | |
| CN103764669A (zh) | 抗炎药物产品 | |
| CA2839986A1 (en) | Targeting the neuromuscular junction for treatment | |
| WO2004050876A1 (fr) | Vaccin genique concernant un adenovirus recombinant convenant a la therapie et la prophylaxie de la maladie d'alzheimer, et utilisation correspondante | |
| CN102666845A (zh) | 磷酸酶和张力蛋白同系物（pten）抑制剂组合物，用途以及方法 | |
| KR20220127880A (ko) | 신경 손상 및 이의 관련 병증 치료 방법 | |
| AU2015287833B2 (en) | Compositions and methods for treating diabetes | |
| KR20230104826A (ko) | 비염증성 식세포작용 유도 활성을 갖는 융합분자 | |
| PT1616007E (pt) | Proteínas inibidoras de uma protease e uso das mesmas | |
| WO2014194427A1 (en) | Targeted iduronate-2-sulfatase fusion proteins | |
| JPH04502260A (ja) | Ｎ―アセチルムラミダーゼ ｍ１ | |
| CN115057945B (zh) | 一种杂合抗菌肽NK-LPd及其基因、载体、制备方法和应用 | |
| JPH0680697A (ja) | ヒト好中球エラスターゼ阻害活性を有する天然型ポリペプチドおよびそれを含有する医薬製剤 | |
| KR20170084653A (ko) | 위장 단백분해효소에 저항성을 갖는 식물 세포 | |
| JP4549666B2 (ja) | 抗体の製造方法 | |
| WO2022218997A1 (en) | Novel universal vaccine presenting system | |
| AU2004316095A1 (en) | Anticancer agent containing BL angiostatin | |
| JP2021520204A (ja) | 酸化ストレスに対する遺伝子療法 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20191113 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20191113 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20201110 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20210208 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20210409 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20210928 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20211223 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20220225 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20220614 |